Molecular choreography in crowded environments: Insights from solvation dynamics

It is important to understand the complex dynamics of proteins in the complex and crowded environments of living cells in order to gain deeper insights into their biological functions. Proteins seldom function alone; rather, they are part of a dense matrix of macromolecules, such as other proteins, nucleic acids, lipids, and carbohydrates, which together form a crowded cellular environment. This macromolecular crowding has a major impact on the behavior of proteins in the cell through the alteration of their folding pathways, conformational stability, hydration structure, as well as intermolecular interactions. All of these factors are important for the regulation of cellular function. Among the diverse experimental strategies available, spectroscopic approaches such as time-resolved fluorescence spectroscopy (TRFS), 2D-infrared (IR), terahertz (THz), and nuclear magnetic resonance (NMR) provide complementary insights into solvation dynamics, hydration structure, and conformational motions. Together, these techniques enable real-time, molecular-level characterization of how crowded environments modulate protein behavior under physiologically relevant conditions.